Crystallization and preliminary X-ray studies of ferric uptake regulator from Magnetospirillum gryphiswaldense

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 68; no. 8; pp. 902 - 905
• Main Authors: Liu, Zhao, Chen, Zhongzhou, Wu, Wei
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.08.2012
• Subjects: Bacteria; Bacterial Proteins - chemistry; Coefficients; Crystallization; Crystallization Communications; Crystallography, X-Ray; Diffraction; ferric uptake regulator; Homeostasis; Iron; Magnetospirillum - chemistry; Magnetospirillum gryphiswaldense MSR-1; magnetotactic bacteria; Regulators; Repressor Proteins - chemistry; Uptakes
• DOI: 10.1107/S1744309112024311
• ISSN: 1744-3091

Magnetosomes in magnetotactic bacteria have been widely used in studies of magnetic domains and in commercial applications. The iron content of magnetotactic bacteria is ∼100 times higher than that of Escherichia coli. Magnetospirillum gryphiswaldense MSR‐1 can still take up iron even at high intracellular concentrations. Ferric uptake regulator (Fur) is a global iron‐responsive regulator that affects magnetosome formation, iron transport and oxygen metabolism. However, the mechanism of iron uptake and homeostasis by M. gryphiswaldense MSR‐1 Fur is not clear. Here, the expression, purification and crystallization of apo and SeMet Fur from M. gryphiswaldense MSR‐1 are reported. The crystals belonged to space group C2. Matthews coefficient analysis and size‐exclusion chromatography showed that the asymmetric unit probably contains one dimer of Fur. Diffraction data were optimized to 1.58 Å resolution for apo Fur and to 1.9 Å resolution for SeMet Fur.